A larger, biologically active protein complex is created when two or more protein subunits come together to form a quaternary structure.
A protein's quaternary structure is formed when several protein chains or subunits come together in a compact configuration. There are separate primary, secondary, and tertiary structures for each of the subunits. Hydrogen bonds and van der Waals forces between nonpolar side chains hold the subunits together.
For a quaternary structure to function as a whole, the subunits must be arranged in a particular way. Any change to the subunits' structure or how they are linked results in noticeable adjustments in biological activity.
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Answer:
Ecological importance
Healthy ecosystems depend on plant and animal species as their foundations. When a species becomes endangered, it is a sign that the ecosystem is slowly falling apart. Each species that is lost triggers the loss of other species within its ecosystem
<span>It is called perception, proprioception, or cognition.
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<span>The role that Stratigraphic dating have played in determining the occurrence of mass extinctions is in its ability to identify different sediment debris. This includes rock and other materials that form or accumulate as the result of natural processes, human activity, or both</span>
Answer:
Golgi apparatus and extracellular matrix
Explanation:
The Golgi complex lies at the heart of the secretory pathway and is responsible for modifying proteins and lipids, as well as sorting newly synthesized molecules to their correct destination. As a consequence of these important roles, any changes in its proteome can negatively affect its function and in turn lead to disease.
Disruption of specific transport steps between the endoplasmic reticulum (ER), Golgi complex, endosomal-lysosomal system and the plasma membrane all can have dramatic consequences on the cell, and increasingly defects in the molecular machinery regulating membrane traffic are being linked to hereditary diseases.
Any changes to the proteome of the Golgi complex would affect its homeostasis and consequently the flux of proteins trafficking through it.
One possible consequence of mutations in Golgi complex proteins is that they cause gross changes in the morphology of the entire organelle and protein mislocalization, which together result in functional problems such as impairment of glycosylation.
Genetic studies of humans and mice continue to highlight the nonredundant mechanical role of components in complexes that anchor cells to extracellular matrices. At the same time, recent data provide exciting insights into, critical roles of transcription factors in regulating differentiation and function of matrix-producing cells.
